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000172163 1001_ $$0P:(DE-HGF)0$$aIsmail, Shehab A$$b0
000172163 245__ $$aArl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo
000172163 260__ $$aBasingstoke$$bNature Publishing Group$$c2011
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000172163 520__ $$aLipidated Rho and Rab GTP-binding proteins are transported between membranes in complex with solubilizing factors called ‘guanine nucleotide dissociation inhibitors’ (GDIs). Unloading from GDIs using GDI displacement factors (GDFs) has been proposed but remains mechanistically elusive. PDEd is a putative solubilizing factor for several prenylated Ras-subfamily proteins. Here we report the structure of fully modified farnesylated Rheb-GDP in complex with PDEd. The structure explains the nucleotide-independent binding of Rheb to PDEd and the relaxed specificity of PDEd. We demonstrate that the G proteins Arl2 and Arl3 act in a GTP-dependent manner as allosteric release factors for farnesylated cargo. We thus describe a new transport system for farnesylated G proteins involving a GDI-like molecule and an unequivocal GDF. Considering the importance of PDEd for proper Ras and Rheb signaling, this study is instrumental in developing a new target for anticancer therapy.
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000172163 7001_ $$0P:(DE-HGF)0$$aChen, Yong-Xiang$$b1
000172163 7001_ $$0P:(DE-HGF)0$$aRusinova, Alexandra$$b2
000172163 7001_ $$0P:(DE-HGF)0$$aChandra, Anchal$$b3
000172163 7001_ $$0P:(DE-HGF)0$$aBierbaum, Martin$$b4
000172163 7001_ $$0P:(DE-Juel1)145165$$aGremer, Lothar$$b5$$ufzj
000172163 7001_ $$0P:(DE-HGF)0$$aTriola, Gemma$$b6
000172163 7001_ $$0P:(DE-HGF)0$$aWaldmann, Herbert$$b7
000172163 7001_ $$0P:(DE-HGF)0$$aBastiaens, Philippe I H$$b8
000172163 7001_ $$0P:(DE-HGF)0$$aWittinghofer, Alfred$$b9$$eCorresponding Author
000172163 773__ $$0PERI:(DE-600)2190276-8$$a10.1038/nchembio.686$$gVol. 7, no. 12, p. 942 - 949$$n12$$p942 - 949$$tNature chemical biology$$v7$$x1552-4469$$y2011
000172163 8564_ $$uhttp://www.nature.com/nchembio/journal/v7/n12/full/nchembio.686.html
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000172163 9141_ $$y2014
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